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Influence of Ovocystatin on Aβ42 soluble oligomeric and fibril formation in in vitro studies

Published online by Cambridge University Press:  27 August 2024

B. Stańczykiewicz*
Affiliation:
1Department of Psychiatry, Wroclaw Medical University
M. Piksa
Affiliation:
2Department of Microbiology
T. Goszczyński
Affiliation:
3Department of Experimental Oncology, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences
K. Gołąb
Affiliation:
4Department of Pharmaceutical Biochemistry, Wroclaw Medical University, Wroclaw, Poland
B. Konopska
Affiliation:
4Department of Pharmaceutical Biochemistry, Wroclaw Medical University, Wroclaw, Poland
A. Zabłocka
Affiliation:
2Department of Microbiology
*
*Corresponding author.

Abstract

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Introduction

Alzheimer’s disease is characterized by the presence of β-amyloid deposits in senile plaques and brain vessels. β-amyloid stimulates the glial release of proinflammatory cytokines, reactive oxygen species (ROS), or nitric oxide (NO), which are potentially toxic to neurons. One potential therapy for Alzheimer’s disease is the use of agents that inhibit the aggregation and formation of insoluble β-amyloid deposits in the brain, or break down the aggregates that have already formed, thus preventing their toxicity.

Objectives

This study aimed to evaluate the effect of ovocystatin on the formation and destabilization of β-amyloid aggregation.

Methods

The effect of ovocystatin on β-amyloid aggregation was determined by Thioflavin T (ThT) Assay and Transmission Electron Microscopy (TEM). The impact on PC12 cell viability was determined by MTT assay.

Results

Ovocystatin can interact directly with Aβ42, inhibiting its aggregation and reducing the toxicity induced by aggregated forms of β-amyloid. All effects are dose-dependent. Additionally, a significant increase in the PC12 cell viability treated simultaneously with Aβ42 and ovocystatin was observed.

Conclusions

Ovocystatin may be an important factor in the prevention and treatment of Alzheimer’s disease by regulating the conversion of monomeric β-amyloid into larger and potentially more toxic particles. However, the mechanisms of inhibition of amyloid fibrillar protein formation and/or destabilization by ovocystatin are still unclear and require further investigation.

Disclosure of Interest

None Declared

Type
Abstract
Creative Commons
Creative Common License - CCCreative Common License - BY
This is an Open Access article, distributed under the terms of the Creative Commons Attribution licence (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted re-use, distribution, and reproduction in any medium, provided the original work is properly cited.
Copyright
© The Author(s), 2024. Published by Cambridge University Press on behalf of European Psychiatric Association
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